ID   NAR3_MOUSE     STANDARD;      PRT;   420 AA.
AC   Q8R2G4; Q8R2F9; Q8R2G0; Q8R2G1; Q8R2G2; Q8R2G3;
DT   15-JUN-2002 (Rel. 41, Created)
DT   15-JUN-2002 (Rel. 41, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Ecto-ADP-ribosyltransferase 3 precursor (EC 2.4.2.31) (NAD(P)(+)--
DE   arginine ADP-ribosyltransferase 3) (Mono(ADP-ribosyl)transferase 3).
GN   ART3.
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=22065832; PubMed=12070318;
RA   Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P.,
RA   Bazan F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
RT   "The family of toxin-related ecto-ADP-ribosyltransferases in humans
RT   and the mouse.";
RL   Protein Sci. 11:1657-1670(2002).
CC   -!- CATALYTIC ACTIVITY: NAD(+) + L-arginine = nicotinamide + N(2)-
CC       (ADP-D-ribosyl)-L-arginine.
CC   -!- SUBCELLULAR LOCATION: Attached to the membrane by a GPI-anchor (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS: 6 isoforms; 1 (shown here), 2, 3, 4, 5 and
CC       6; are produced by alternative splicing.
CC   -!- PTM: TWO DISULFIDE BONDS ARE PRESENT (BY SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO THE ARG-SPECIFIC ADP-RIBOSYLTRANSFERASE
CC       FAMILY.
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DR   EMBL; AJ311768; CAC84539.1; -.
DR   EMBL; AJ311769; CAC84526.1; -.
DR   EMBL; AJ311770; CAC84540.1; -.
DR   EMBL; AJ311771; CAC84541.1; -.
DR   EMBL; AJ311772; CAC84542.1; -.
DR   EMBL; AJ311773; CAC84543.1; -.
DR   InterPro; IPR000768; ART_family.
DR   Pfam; PF01129; ART; 1.
KW   Transferase; Glycosyltransferase; Glycoprotein; NAD; Signal;
KW   GPI-anchor; Alternative splicing.
FT   SIGNAL        1     26       POTENTIAL.
FT   CHAIN        27    381       ECTO-ADP-RIBOSYLTRANSFERASE 3.
FT   PROPEP      382    420       HYDROPHOBIC, REMOVED DURING MATURATION
FT                                (BY SIMILARITY).
FT   ACT_SITE    228    228       BY SIMILARITY.
FT   CARBOHYD    182    182       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    247    247       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    355    355       N-LINKED (GLCNAC...) (POTENTIAL).
FT   LIPID       381    381       GPI-ANCHOR (BY SIMILARITY).
FT   VARSPLIC    303    314       MISSING (IN ISOFORM 2, ISOFORM 4 AND
FT                                ISOFORM 6).
FT   VARSPLIC    343    420       TEVEERPTILVRNTSFSLKNALKYKTVKLILFFIKSSRSGS
FT                                RSEIPSLCILWQYAPSISHGIHHFTRCFCCKLHRAIA ->
FT                                LQVWFQVRNPIPLHPLAIRSFHQSWHPPFYSLLLL (IN
FT                                ISOFORM 2 AND ISOFORM 3).
FT   VARSPLIC    353    420       VRNTSFSLKNALKYKTVKLILFFIKSSRSGSRSEIPSLCIL
FT                                WQYAPSISHGIHHFTRCFCCKLHRAIA -> LQVWFQVRNP
FT                                IPLHPLAIRSFHQSWHPPFYSLLLL (IN ISOFORM 4).
FT   VARSPLIC    271    420       EYIDPRYLYNPGEYTLLQTTQIWTIRSLKTLVPGIKPWAPC
FT                                KLVGTTLTLTECQKLKCYKQRKILSCRMKSLTEVEERPTIL
FT                                VRNTSFSLKNALKYKTVKLILFFIKSSRSGSRSEIPSLCIL
FT                                WQYAPSISHGIHHFTRCFCCKLHRAIA -> GRNNLDPDRM
FT                                PEIKVLQTEENPLLPDEKPDRSRGKANNPTPGLVPGPKSHP
FT                                SASSGNTLLPSVMASTILLVASAVNFIEL (IN ISOFORM
FT                                5).
SQ   SEQUENCE   420 AA;  48302 MW;  DA013A5718DC2FD7 CRC64;
     MKMGHFEMVT TLLAAAVLMD IFQVKAEVLD MAENAFDDEY LKCKSRMESK YIPQMKREEW
     ANDALLRMVW DNAEIQWEAR KAQLFLPRNF KDTYGIALTA YVNEAQEQTS FYHTFSSAVK
     MAGLSRRRYI YNFPFKAFHF YLVRALQLLR RPCEKSYKTV VYSTSPDISF TFGEQNQARL
     GNFTLAYSAK PETADNQRVL TIQTCFGVAV GKFLNKEDDS VVLIPLSEVF QVSRKGTSND
     LVLQSINSTC SYYECAFLGG LKTENCIANA EYIDPRYLYN PGEYTLLQTT QIWTIRSLKT
     LVPGIKPWAP CKLVGTTLTL TECQKLKCYK QRKILSCRMK SLTEVEERPT ILVRNTSFSL
     KNALKYKTVK LILFFIKSSR SGSRSEIPSL CILWQYAPSI SHGIHHFTRC FCCKLHRAIA
//